NAVIGATION

The absence of disease does not necessarily mean the presence of wellness. One may not be experiencing symptoms of disease and yet the body may be beginning to gradually break down due to lack of nutrition, exercise and a healthy life style. Eventually such gradual breakdown begins to manifest itself in a variety of disorders which we attach various names to such as arthritis, diabetes, cancer, etc.

In years past, food was thought to be nothing more than a source of calories for production of energy for the body. We now understand that food contains thousands of elements that must be present if the body is to function at optimal level. The quality of food is a measurement of nutritional density. Foods that are high in vitamins, minerals, amino acids, enzymes and a variety of other micronutrients are said to be nutritionally dense. It is those kinds of foods that we need to maximize in our diet.

The nutritional calorie is the amount of heat required to raise approximately one quart of water two degrees Fahrenheit. Nutritional density is defined as the relative amount of vitamins, minerals, etc, per 1,000 calories of food. The higher the micro nutritional density of a food, the greater it will support the health of the body. Food low in nutritional density is defined as empty calorie food. In order for food calories to be optimally utilized by the body, they must be metabolized in the presence of a wide variety of micro nutrients.

THE MACRO NUTRIENTS:

The three macronutrients of protein, carbohydrate and fat are the source of calories for the body’s production of energy. Protein and carbohydrate have four calories per gram of potential energy. Fat has nine calories per gram of potential energy. As you can see, fat is more than twice as energy dense as protein or carbohydrate. Unfortunately, most fat is micronutrient poor. Therefore, diets high in fat tend to be calorie dense and micronutrient poor.

We will begin our discussion of macro nutrients by looking at the role of protein in human health.

PROTEIN:

Our bodies are made up of hundreds of proteins which are individually made up of a little over 20 different amino acids of which eight (called essential amino acids) must be derived from the diet while the rest, (called non-essential amino acids) are made by the body. Protein contains high levels of the element nitrogen. Eighty percent of the air we breathe is nitrogen gas. Nitrogen is extremely stable which prevents it from easily being taken into the food chain. For it to be utilized in the making of proteins, nitrogen must be either reduced to substances like ammonia or to nitrates. One way this is accomplished is through a process called nitrogen fixation which can only occur in plants through the activity of certain bacteria.

In an effort to increase available protein in the food supply, modern agriculture has for a number of years been adding chemical nitrogen fertilizers such as ammonium salts to the soil. While this practice has increased the protein content of plants, it has also led to higher acidity of the soil which has reduced the release of minerals into the soil from ground water and other sources. Therefore, there has been a marked reduction in the trace mineral content of many foods in recent years.

We obtain protein in our bodies by eating plants or the flesh and other derivatives of animals that eat plants. Such ingested protein is broken down by the digestive process into their constituent amino acids which pass into the blood stream and travel to the liver. The liver rearranges the amino acids in various ways to form protein building blocks for repair and maintenance of tissues through the body. The proteins make by the liver are matched to the proteins out of which your body is made and this process is regulated by your bodies DNA. This is why no two people are exactly the same as to the makeup of the particular proteins that make up their body.

Our body’s proteins are structural, catalytic and regulatory. All three of these classes of protein are synthesized within cells called ribosome’s as directed by DNA within the nucleus of such cells.

Structural proteins:

Structural proteins, such as collagen and elastin, make up the materials of tendons, bone, ligaments and other connective tissue. Elastin is a protein that makes up the walls of the arteries and gives them their ability to stretch and therefore respond to differences in blood pressure. This protein requires large amounts of the essential amino acid lysine. The structural protein keratin is found in abundance in nails and hair and requires a lot of the sulfur amino acid cysteine.

Collagen protein virtually holds our bodies together. It requires the combining of the amino acid proline and vitamin C to produce hydroxyproline. When a person is deficient in vitamin C, he cannot produce adequate levels of hydroxyproline and collagen is manufactured imperfectly. This can lead to bleeding gums, increased capillary fragility, easy bruising and other connective tissue problems.

Catalytic proteins:

Catalytic proteins are enzymes that control the rate of all biochemical reactions in the body. Digestive enzymes break down the food we eat into usable elements. Antioxidant enzymes protect our cells from oxidation and free radical damage. Other enzymes are involved in various metabolic processes. The activity of enzymes is facilitated by various vitamins and minerals which act as co-factors and are classified as coenzymes. For example, the mineral magnesium participates in nearly 80% of enzyme mediated reactions in the body. Therefore magnesium deficiency can produce widespread symptoms of malfunction. The B complex of vitamins are converted to numerous coenzymes that facilitate specific enzyme activities. Deficiency of one or more of the B Vitamins will adversely affect the function of enzymes and therefore the facilitation of various biochemical reactions.

Regulatory proteins:

Regulatory proteins are hormones which regulate various body functions. Insulin and glucagon, which are both produced by the pancreas gland, are good examples of hormone proteins. Both these hormones play a vital role in regulating blood sugar levels. Insulin responds to carbohydrate. When you eat carbohydrate, which digests into glucose, your pancreas releases insulin which, with the help of the mineral chromium, removes glucose from the blood into the cells and thus lowers blood sugar. The cells then use the glucose calories to produce energy. Insulin will convert excess glucose into stored carbohydrate called glycogen, and fat. Glucagon responds to protein, not carbohydrate, and works in opposition to insulin. When you eat protein, it stimulates the pancreas to produce the hormone glucagon which releases glycogen and fat stored in adipose tissue as a result of the activity of insulin. As you can see, both these hormones work to regulate blood sugar levels so that such levels are neither to high or to low.

Protein requirements:

The recommended daily protein requirements for humans are derived from "ideal body weight". The ideal body weight is calculated based on height and varies slightly for men and women. Our protein requirements can also be expressed in terms of total caloric intake. The world health organization and many national health agencies have independently conducted studies, which (even though they differ slightly) all conclude our daily protein requirement should be between 10% to 15% of our daily caloric intake. The daily protein requirement is usually expressed in grams. You can have your daily protein requirements automatically figured out for you by going to http://www.indoorclimbing.com/Protein_Requirement.html.

Most Americans get enough protein on a daily basis to facilitate maintenance, repair and replacement of protein requiring tissues. For individuals who work out on a regular basis, there may be a need for additional protein to prevent muscle wasting. Muscle tissue is made up primarily of protein. When you work out, especially if you lift weights, you can be at risk for breaking down protein faster than you are replacing it. This leads to a reduction in muscle tissue which is the opposite of what you are trying to accomplish through exercise. It is therefore important that you eat not only sufficient amounts of protein but also complex carbohydrates to insure that the body doesn’t go to using protein for energy production while working out. One must also be careful, however, not to overdo it with protein. Studies have shown that excessive amounts of protein intake can increase bone loss and facilitate osteoporosis. This is due to the high levels of phosphorous and sulfur in protein which increases the acidity of the blood leading to greater loss of calcium in the urine.

The urea cycle:

As explained earlier, protein is very high in nitrogen. The urea cycle is the mechanism by which the body gets rid of excessive nitrogen. This cycle operates predominately in the liver where ammonia is converted to urea through the action of certain amino acids and this urea is then eliminated in the urine. Ammonia is manufactured as a by-product of used up amino acids and proteins being reduced to nitrogen which then combines with hydrogen to form ammonia. Failure of this process to adequately reduce ammonia levels can lead to its release from the liver into the blood with subsequent damage to tissues throughout the body but especially in the brain. Excessive protein in the diet leading to excessive urea production is also toxic to the kidneys. It has been found that a protein restricted diet can reduce the progression of kidney disease and effectively bring down levels of ammonia.

Protein digestion:

When you eat a meal, the protein from that meal begins to digest in the stomach where hydrochloric acid and the enzyme pepsin begin to break it down into individual amino acids. This partially digested protein then travels to the duodenum, which is the upper part of the small intestine, where its digestion continues by the action of bicarbonate and a group of enzymes secreted by the pancreas called proteases. What began as complex dietary proteins are broken down into individual amino acids which travel via the blood stream to the liver where they are rearranged and sent throughout the body to build and maintain body tissues.

Some proteins are difficult to digest and don’t always break down into their individual amino acids. When such partially digested proteins enter the blood stream, they can create allergic reactions. An allergic reaction is the body’s immune system treating something in the body as a foreign substance which results in unwanted symptoms.

One allergy producing protein can be gluten. Gluten is an elastic, rubbery protein present in wheat, rye, barley and to a lesser degree in oats. It binds the dough in foods such as bread and other baked goods. Rice and corn do not contain gluten. A gluten allergy called celiac disease is an autoimmune condition that causes damage to the tiny finger like projections lining the small intestine called villi. Villi are where nutrients are absorbed into the blood stream. Symptoms can include chronic abdominal bloating and pain, diarrhea, constipation, weight loss and sometimes a blistery rash. Because this disease creates poor absorption of nutrients, symptoms of fatigue and depression are often present. Allergy to gluten can be determined by a blood test that measures for antibodies to gluten.

A protein found in dairy products called casein is a problem for some as it can produce allergic reactions such as nausea, vomiting, diarrhea and abdominal cramps, hives etc. As with gluten, a test for antibodies to casein can determine if there is an allergy to this protein.

Signs of poor protein digestion include bloating, flatulence and heartburn. If you experience these symptoms on a regular basis, taking a digestive supplement such as hydrochloric acid (HCL) with pepsin and/or an enzyme product high in proteases may be helpful. Sometimes taking a little apple cider vinegar with or before eating protein will be just enough to increase the acidity of the stomach resulting in better protein breakdown.